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UniProtKB - Q12373 (HIF1_YEAST)

Entry version 145 (08 May 2019)
Sequence version 1 (01 Nov 1996)
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Protein

HAT1-interacting factor 1

Gene

HIF1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Histone H3 and H4 specific chaperone component of the nuclear histone acetyltransferase B (HAT-B) complex. Involved in chromatin assembly and telomere silencing.2 Publications

Miscellaneous

Present with 4550 molecules/cell in log phase SD medium.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • histone binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChromatin regulator
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		YEAST:G3O-32126-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
HAT1-interacting factor 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:HIF1
Ordered Locus Names:YLL022C
ORF Names:L1205
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:YLL022C

Saccharomyces Genome Database

More...SGDi		S000003945 HIF1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi80 – 158Missing : Abolishes interaction with heterotetrameric histone H3 and H4 and with dimeric histone H2A and H2B. 1 PublicationAdd BLAST79
Mutagenesisi85 – 198Missing : Abolishes interaction with histones H2A, H2B, H3 and H4. 2 PublicationsAdd BLAST114
Mutagenesisi95 – 158Missing : Mildly decreases interaction with heterotetrameric histone H3 and H4 and abolishes interaction with dimeric histone H2A and H2B. 1 PublicationAdd BLAST64
Mutagenesisi135 – 158Missing : Minimal decrease of interaction with heterotetrameric histone H3 and H4 and with dimeric histone H2A and H2B. 2 PublicationsAdd BLAST24
Mutagenesisi248E → A: Strongly reduces affinity for dimeric histone H2A and H2B; when associated with A-250; A-288; A-291 and 332-A--A-342. 1 Publication1
Mutagenesisi250E → A: Strongly reduces affinity for dimeric histone H2A and H2B; when associated with A-248; A-288; A-291 and 332-A--A-342. 1 Publication1
Mutagenesisi288D → A: Strongly reduces affinity for dimeric histone H2A and H2B; when associated with A-248; A-250; A-291 and 332-A--A-342. 1 Publication1
Mutagenesisi291R → A: Strongly reduces affinity for dimeric histone H2A and H2B; when associated with A-248; A-250; A-288 and 332-A--A-342. 1 Publication1
Mutagenesisi332 – 342QIQDDIDEVQE → AIQAAIDAVQA: Strongly reduces affinity for dimeric histone H2A and H2B; when associated with A-248; A-250; A-288 and A-291. 1 PublicationAdd BLAST11

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002277311 – 385HAT1-interacting factor 1Add BLAST385

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei174PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q12373

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q12373

PRoteomics IDEntifications database

More...PRIDEi		Q12373

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q12373

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:27618665). The homodimer interacts with a histone tetramer containing H3 and H4; the interaction is direct (PubMed:24946827, PubMed:27618665). The homodimer interacts with heterodimeric histone H2A and H2B; the interaction is direct (PubMed:24946827, PubMed:27618665).

Component of the nuclear histone acetyltransferase B (HAT-B) complex composed of at least HAT1, HAT2 and HIF1 (PubMed:14761951, PubMed:15099519). Does not interact with HAT1 in the absence of HAT2 (PubMed:14761951, PubMed:24946827).

Interacts with histones H3 and H4 in a HAT1/HAT2 dependent manner (PubMed:14761951, PubMed:15099519). Interaction with heterotetrameric histone H3 and H4 precludes interaction with dimeric histone H2A and H2B, irrespective of the fact that their binding involves non-identical regions of the protein (PubMed:24946827, PubMed:27618665).

4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		31231, 56 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1682 Histone acetyltransferase B

Database of interacting proteins

More...DIPi		DIP-6442N

Protein interaction database and analysis system

More...IntActi		Q12373, 6 interactors

Molecular INTeraction database

More...MINTi		Q12373

STRING: functional protein association networks

More...STRINGi		4932.YLL022C

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1385
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q12373

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati186 – 220TPR 1Sequence analysisAdd BLAST35
Repeati229 – 262TPR 2Sequence analysisAdd BLAST34
Repeati289 – 322TPR 3Sequence analysisAdd BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni80 – 199Important for interaction with heterotetrameric histone H3 and H4 and for interaction with dimeric histone H2A and H2B2 PublicationsAdd BLAST120
Regioni248 – 332Interaction with dimeric histone H2A and H2B1 PublicationAdd BLAST85

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi97 – 184Glu-richAdd BLAST88

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal TPR repeat region contains an acidic patch that is important for interaction with histones (PubMed:24946827, PubMed:27618665). A C-terminal, highly polar region mediates interaction with dimeric histone H2A and H2B, but is not involved in interaction with heterotetrameric histone H3 and H4 (PubMed:27618665).2 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the NASP family.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q12373

KEGG Orthology (KO)

More...KOi		K11372

Identification of Orthologs from Complete Genome Data

More...OMAi		TIFAQAV

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.25.40.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011990 TPR-like_helical_dom_sf

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q12373-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLRAEDVLA NGTSRHKVQI DMERQVQIAK DLLAQKKFLE AAKRCQQTLD 
        60         70         80         90        100
SLPKDGLLPD PELFTIFAQA VYNMEVQNSG NLFGDALLAG DDGSGSESES 
       110        120        130        140        150
EPESDVSNGE EGNENGQTEI PNSRMFQFDQ EEEDLTGDVD SGDSEDSGEG 
       160        170        180        190        200
SEEEEENVEK EEERLALHEL ANFSPANEHD DEIEDVSQLR KSGFHIYFEN 
       210        220        230        240        250
DLYENALDLL AQALMLLGRP TADGQSLTEN SRLRIGDVYI LMGDIEREAE 
       260        270        280        290        300
MFSRAIHHYL KALGYYKTLK PAEQVTEKVI QAEFLVCDAL RWVDQVPAKD 
       310        320        330        340        350
KLKRFKHAKA LLEKHMTTRP KDSELQQARL AQIQDDIDEV QENQQHGSKR 
       360        370        380 
PLSQPTTSIG FPALEKPLGD FNDLSQLVKK KPRRH
Length:385
Mass (Da):43,428
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB280CFCCB6896506
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X97560 Genomic DNA Translation: CAA66169.1
Z73127 Genomic DNA Translation: CAA97470.1
BK006945 Genomic DNA Translation: DAA09298.1

Protein sequence database of the Protein Information Resource

More...PIRi		S64770

NCBI Reference Sequences

More...RefSeqi		NP_013078.1, NM_001181842.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YLL022C_mRNA; YLL022C_mRNA; YLL022C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		850638

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YLL022C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97560 Genomic DNA Translation: CAA66169.1
Z73127 Genomic DNA Translation: CAA97470.1
BK006945 Genomic DNA Translation: DAA09298.1
PIRiS64770
RefSeqiNP_013078.1, NM_001181842.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NQ0X-ray2.10A1-385[»]
5BT1X-ray2.62A/B1-385[»]
SMRiQ12373
ModBaseiSearch...

Protein-protein interaction databases

BioGridi31231, 56 interactors
ComplexPortaliCPX-1682 Histone acetyltransferase B
DIPiDIP-6442N
IntActiQ12373, 6 interactors
MINTiQ12373
STRINGi4932.YLL022C

PTM databases

iPTMnetiQ12373

Proteomic databases

MaxQBiQ12373
PaxDbiQ12373
PRIDEiQ12373

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLL022C_mRNA; YLL022C_mRNA; YLL022C
GeneIDi850638
KEGGisce:YLL022C

Organism-specific databases

EuPathDBiFungiDB:YLL022C
SGDiS000003945 HIF1

Phylogenomic databases

InParanoidiQ12373
KOiK11372
OMAiTIFAQAV

Enzyme and pathway databases

BioCyciYEAST:G3O-32126-MONOMER

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q12373

Family and domain databases

Gene3Di1.25.40.10, 2 hits
InterProiView protein in InterPro
IPR011990 TPR-like_helical_dom_sf

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHIF1_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q12373
Secondary accession number(s): D6VXY2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: November 1, 1996
Last modified: May 8, 2019
This is version 145 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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